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Database: UniProt
Entry: B9KEK7
LinkDB: B9KEK7
Original site: B9KEK7 
ID   UNG_CAMLR               Reviewed;         229 AA.
AC   B9KEK7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   19-FEB-2014, entry version 34.
DE   RecName: Full=Uracil-DNA glycosylase;
DE            Short=UDG;
DE            EC=3.2.2.27;
GN   Name=ung; OrderedLocusNames=Cla_0126;
OS   Campylobacter lari (strain RM2100 / D67 / ATCC BAA-1060).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=306263;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM2100 / D67 / ATCC BAA-1060;
RX   PubMed=18713059; DOI=10.1089/fpd.2008.0101;
RA   Miller W.G., Wang G., Binnewies T.T., Parker C.T.;
RT   "The complete genome sequence and analysis of the human pathogen
RT   Campylobacter lari.";
RL   Foodborne Pathog. Dis. 5:371-386(2008).
CC   -!- FUNCTION: Excises uracil residues from the DNA which can arise as
CC       a result of misincorporation of dUMP residues by DNA polymerase or
CC       due to deamination of cytosine (By similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolyzes single-stranded DNA or mismatched
CC       double-stranded DNA and polynucleotides, releasing free uracil.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase family.
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DR   EMBL; CP000932; ACM63492.1; -; Genomic_DNA.
DR   RefSeq; YP_002574743.1; NC_012039.1.
DR   ProteinModelPortal; B9KEK7; -.
DR   STRING; 306263.Cla_0126; -.
DR   EnsemblBacteria; ACM63492; ACM63492; Cla_0126.
DR   GeneID; 7411358; -.
DR   KEGG; cla:Cla_0126; -.
DR   PATRIC; 20060695; VBICamLar15090_0126.
DR   eggNOG; COG0692; -.
DR   HOGENOM; HOG000229528; -.
DR   KO; K03648; -.
DR   OMA; AGKEIYP; -.
DR   OrthoDB; EOG6MSS63; -.
DR   ProtClustDB; PRK05254; -.
DR   BioCyc; CLAR306263:GH7X-126-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.470.10; -; 1.
DR   HAMAP; MF_00148; UDG; 1.
DR   InterPro; IPR018085; Ura-DNA_Glyclase_AS.
DR   InterPro; IPR002043; Ura_DNA_glycsylse.
DR   InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR   PANTHER; PTHR11264; PTHR11264; 1.
DR   Pfam; PF03167; UDG; 1.
DR   SMART; SM00986; UDG; 1.
DR   SUPFAM; SSF52141; SSF52141; 1.
DR   TIGRFAMs; TIGR00628; ung; 1.
DR   PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; DNA damage; DNA repair; Glycosidase;
KW   Hydrolase.
FT   CHAIN         1    229       Uracil-DNA glycosylase.
FT                                /FTId=PRO_1000199774.
FT   ACT_SITE     71     71       Proton acceptor (By similarity).
SQ   SEQUENCE   229 AA;  26020 MW;  D9F609D093DE0CC6 CRC64;
     MDICLEKIKI EQTWKEFLKD EFLKPYFLEI KTHYINALNE GKTIYPPANL IFNAFNLAPL
     QDLKIILLGQ DPYHNPHQAM GLSFSVPMGV KIPPSLLNIY KELQNDLNIP MAKHGDLSKW
     AKQGVLLLNS ILSVEANKPA SHAHFGWQKF TDAVISKLSD EKEGLVFLLW GNYAKNKKVL
     INPQKHFILE AAHPSPLARN AFLGCKHFSK SNEILLKLGK SPIDWNLNL
//
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